2022 Fiscal Year Research-status Report
Elucidation of the Far3- and Far7-mediated regulatory mechanism of mitochondrial autophagy in yeast
| Project/Area Number |
22K15058
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| Research Institution | Niigata University |
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Principal Investigator |
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| Project Period (FY) |
2022-04-01 – 2024-03-31
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| Keywords | Mitophagy / Atg32 / Ppg1 / The Far complex / Yeast / Autophagy |
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| Outline of Annual Research Achievements |
This study investigates mitophagy, which maintains mitochondrial quality and quantity. The Far complex interacts with a receptor protein Atg32 to facilitate mitophagy by phosphorylating it. However, the mechanism of this interaction is still unclear. The study found that Far3/7 do not directly interact with Atg32, but they are needed for Far8-Atg32 interaction. Substitution mutants of Far3/7 phosphorylation sites, expression, degradation, and a set of kinases involved in autophagy did not influence the Atg32-Far complex interaction. The study suggests exploring other known interacting partners of the Far complex and Atg32 and investigating the role of other post-translational modifications, as well as the effect of cellular stress and nutrient availability on the Atg32-Far8 interaction.
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| Current Status of Research Progress |
Current Status of Research Progress
3: Progress in research has been slightly delayed.
Reason
I had some problems with protein expression of plasmids for Far3 and Far7 substitution mutants and I had to change strategy to genomic integration of
Far3 and Far7 substitution mutations, which takes longer time compared to construction of plasmids with substitution mutations. Additionally, Far3 and Far7 phosphotylation proved not to be involved in Atg32-Far complex interaction, so I must find a new way which regulates Atg32-Far complex interaction.
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| Strategy for Future Research Activity |
These results suggests exploring other known interacting partners of the Far complex and Atg32 and investigating the role of other post-translational modifications (acetylation, methylation, ubiquitination, sumoylation, and glycosylation), as well as the effect of cellular stress and nutrient availability on the Atg32-Far8 interaction. The regulation of mitophagy is complex and requires further research to understand the mechanisms involved.
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